Linked Life Data

11002189

Source:http://linkedlifedata.com/resource/pubmed/id/11002189

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2000-10-5
pubmed:abstractText
The effect of ionic strength of the reaction medium on the pH optimum, specificity, and mechanism of action of the acid DNase isolated from mature eggs of the sea urchin Strongylocentrotus intermedius was studied. Changes in ionic strength of the reaction medium caused a displacement of the pH optimum of the enzyme to acidity or alkalinity. The region and range of this displacement depended on the buffer used and on the substrate structure. For single-stranded, duplex, and supercoiled forms of DNA, the pH optimum displacements were 1.0, 1.4, and 2.0 pH units, respectively. The pH optimum displacement changed the mechanism of action of the enzyme. Under optimum pH conditions, the enzyme cleaved supercoiled DNA only by the double-hit mechanism, and fragments of duplex DNA resulted due to the coincidence of breaks in opposite chains. On pH displacement to acidity, the enzyme acted by the mixed mechanism (single- and double-hit). And the quantitative ratio of products of the enzymatic hydrolysis of supercoiled DNA was significantly changed depending on the pH displacement to acidity or to alkalinity. The findings are explained by the effect of salt-dependent electrostatic interactions during the formation of a nonspecific DNA-enzyme complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2979
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
952-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Effect of ionic strength on the pH optimum, specificity, and mechanism of action of acid DNase from mature eggs of the sea urchin Strongylocentrotus intermedius.
pubmed:affiliation
Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok, 690022, Russia. piboc@stl.ru
pubmed:publicationType
Journal Article